Venom composition of the Iberian adder (Vipera seoanei) from northern Portugal reveals limited sex and size variation

Posted by
  Venom composition of the Iberian adder (Vipera seoanei) from northern Portugal reveals limited sex and size variation Abstract Snake venom is a complex and dynamic ecological trait, with high potential for intraspecific variation. In this study, the venom composition of the Iberian adder ( Vipera seoanei ) from the Peneda Mountains of northern Portugal was investigated to explore whether venom varies with body size and sex. Venom proteomes from six individuals representing juvenile, subadult, and adult males and females were characterised using LC–MS/MS, while individual variation was assessed from SDS–PAGE profiles of 18 snakes. LC–MS/MS identified 144 proteins, dominated by phospholipases A 2 (PLA 2 ), snake venom serine proteases (svSP), and C-type lectin-related proteins (CTL). Descriptive comparisons revealed contrasting individual profiles, particularly between the juvenile male, characterised by high svSP and svMP abundance, and the juvenile female, characterised by high ...

Peptidomics and pharmacological profiling of Odontobuthus doriae (Buthidae) scorpion venom at the kappa opioid receptor

Posted by

 

Peptidomics and pharmacological profiling of Odontobuthus doriae (Buthidae) scorpion venom at the kappa opioid receptor

Abstract

Scorpion venoms are rich in bioactive peptides, many of which act on ion channels and neurotransmitter systems, yet their capacity to interact with G protein-coupled receptors (GPCRs) has been largely unexplored. Here, we profiled the venom peptides of five species in the family Buthidae and evaluated their activity at the kappa opioid receptor (KOR). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) revealed species-specific peptide fingerprints in the mass range between 2.5 and 4 kDa, underscoring interspecies peptide toxin variation. Following pre-purification by solid-phase extraction, radioligand displacement assays demonstrated that fractions from Odontobuthus doriae bound to KOR, with Od-e (36% acetonitrile) and Od-f (45% acetonitrile) displacing ~ 35–40% of [³H]-diprenorphine. However, BRET-based functional assays demonstrated only weak receptor activation, suggesting that these peptides may function as partial agonists or antagonists rather than full agonists. Collectively, these findings highlight scorpion venoms as a previously underexplored source of opioid receptor-interacting peptides. Systematic investigation of their structural diversity and pharmacological profiles in the future may not only expand our understanding of venom evolution but also provide novel scaffolds for GPCR ligand discovery and potential analgesic development.

Abdollahnia, A., Bata, B. B., Fraunhofer, A., Hermes, J., Atashi, J., Ghassempour, A., & Gruber, C. W. (2026). Peptidomics and pharmacological profiling of Odontobuthus doriae (Buthidae) scorpion venom at the kappa opioid receptor. Scientific Reports. https://doi.org/10.1038/s41598-025-31108-9